Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q12WX1 (Q12WX1_METBU) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
CCA-adding enzyme HAMAP-Rule MF_01264

EC=2.7.7.72 HAMAP-Rule MF_01264
Alternative name(s):
CCA tRNA nucleotidyltransferase HAMAP-Rule MF_01264
tRNA CCA-pyrophosphorylase HAMAP-Rule MF_01264
tRNA adenylyl-/cytidylyl- transferase HAMAP-Rule MF_01264
tRNA nucleotidyltransferase HAMAP-Rule MF_01264
tRNA-NT HAMAP-Rule MF_01264
Gene names
Name:cca HAMAP-Rule MF_01264 EMBL ABE52055.1
Ordered Locus Names:Mbur_1130 EMBL ABE52055.1
OrganismMethanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M) [Complete proteome] [HAMAP] EMBL ABE52055.1
Taxonomic identifier259564 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanococcoides

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate By similarity. HAMAP-Rule MF_01264

Catalytic activity

A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate. HAMAP-Rule MF_01264

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01264

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01264

Miscellaneous

A single active site specifically recognizes both ATP and CTP and is responsible for their addition By similarity. HAMAP-Rule MF_01264

Sequence similarities

Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily. HAMAP-Rule MF_01264

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding641Magnesium By similarity HAMAP-Rule MF_01264
Metal binding661Magnesium By similarity HAMAP-Rule MF_01264
Metal binding1181Magnesium By similarity HAMAP-Rule MF_01264
Binding site521ATP or CTP By similarity HAMAP-Rule MF_01264
Binding site551ATP or CTP By similarity HAMAP-Rule MF_01264
Binding site1411ATP or CTP By similarity HAMAP-Rule MF_01264
Binding site1601ATP or CTP By similarity HAMAP-Rule MF_01264
Binding site1691ATP or CTP By similarity HAMAP-Rule MF_01264

Sequences

Sequence LengthMass (Da)Tools
Q12WX1 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 5B4AD00060D50EEB

FASTA44650,467
        10         20         30         40         50         60 
MESLKKSILE KIKPTEKERE HLTKVADELM YKIDCLTFKV GLVGVKTQLV GSAARGTWIS 

        70         80         90        100        110        120 
GTHDLDIFIT FPDDTSREDL ESYGLSVGRQ VAKEAEHWDE HYAEHPYVKM RYKGFDVDLV 

       130        140        150        160        170        180 
PCYSVSSASS IISAVDRTPF HNEFIKANLN GLEDEVLLLK QFMRGTGVYG SELKTEGFSG 

       190        200        210        220        230        240 
YLTELLVINY GSFEKVLEAA SNWRPGLLLD ILEHGKLKFE DPLVVIDPTD PKRNVAAALS 

       250        260        270        280        290        300 
LDKFCTFVDM ARSFLCNPDE SMFFSSLIPP ISDNEIVERL EKKGSSLLAI VFKTPDVVDD 

       310        320        330        340        350        360 
IFYPQFAKME NSVVPMLDKN EFTVLKAGKW SGEDSVVMLE LMSGTLPNVK MHRGPPVWVR 

       370        380        390        400        410        420 
DHAEKFRDKY VDNEDAYSFT IKDGFYVAEI PRKHISAVEL LKKELANCSL GKHISKSVKE 

       430        440 
GFEILEGEQV LELKEDGFRS YLKSWL 

« Hide

References

[1]"Complete sequence of Methanococcoides burtonii DSM 6242."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Anderson I., Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6242 / NBRC 107633 / OCM 468 / ACE-M.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000300 Genomic DNA. Translation: ABE52055.1.
RefSeqYP_565805.1. NC_007955.1.

3D structure databases

ProteinModelPortalQ12WX1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING259564.Mbur_1130.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE52055; ABE52055; Mbur_1130.
GeneID3997737.
KEGGmbu:Mbur_1130.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1746.
HOGENOMHOG000226400.
KOK07558.
OMADRTPFHN.
ProtClustDBPRK13300.

Enzyme and pathway databases

BioCycMBUR259564:GHBZ-1151-MONOMER.

Family and domain databases

HAMAPMF_01264. CCA_arch.
InterProIPR008229. CCA-adding_arc.
IPR002934. Nucleotidyltransferase.
IPR011068. NuclTrfase_I_C.
IPR015329. tRNA_NucTransf2.
[Graphical view]
PfamPF01909. NTP_transf_2. 1 hit.
PF09249. tRNA_NucTransf2. 1 hit.
[Graphical view]
PIRSFPIRSF005335. CCA_arch. 1 hit.
SUPFAMSSF55003. SSF55003. 1 hit.
TIGRFAMsTIGR03671. cca_archaeal. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ12WX1_METBU
AccessionPrimary (citable) accession number: Q12WX1
Entry history
Integrated into UniProtKB/TrEMBL: August 22, 2006
Last sequence update: August 22, 2006
Last modified: February 19, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)